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JXB Advance Access published online on January 6, 2009
Journal of Experimental Botany, doi:10.1093/jxb/ern311
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

A green fluorescent protein fused to rice prolamin forms protein body-like structures in transgenic rice

Yuhi Saito1, Koichi Kishida1, Kenji Takata1, Hideyuki Takahashi1, Takeaki Shimada1, Kunisuke Tanaka1, Shigeto Morita1,2, Shigeru Satoh1,2 and Takehiro Masumura1,2,*

1Laboratory of Genetic Engineering, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Shimogamo, Kyoto 606-8522, Japan
2Kyoto Prefectural Institute of Agricultural Biotechnology, Kitainayazuma, Seika-cho, Soraku-gun, Kyoto 619-0244, Japan

* To whom correspondence should be addressed. E-mail: masumura{at}kpu.ac.jp

Prolamins, a group of rice (Oryza sativa) seed storage proteins, are synthesized on the rough endoplasmic reticulum (ER) and deposited in ER-derived type I protein bodies (PB-Is) in rice endosperm cells. The accumulation mechanism of prolamins, which do not possess the well-known ER retention signal, remains unclear. In order to elucidate whether the accumulation of prolamin in the ER requires seed-specific factors, the subcellular localization of the constitutively expressed green fluorescent protein fused to prolamin (prolamin–GFP) was examined in seeds, leaves, and roots of transgenic rice plants. The prolamin–GFP fusion proteins accumulated not only in the seeds but also in the leaves and roots. Microscopic observation of GFP fluorescence and immunocytochemical analysis revealed that prolamin–GFP fusion proteins specifically accumulated in PB-Is in the endosperm, whereas they were deposited in the electron-dense structures in the leaves and roots. The ER chaperone BiP was detected in the structures in the leaves and roots. The results show that the aggregation of prolamin–GFP fusion proteins does not depend on the tissues, suggesting that the prolamin–GFP fusion proteins accumulate in the ER by forming into aggregates. The findings bear out the importance of the assembly of prolamin molecules and the interaction of prolamin with BiP in the formation of ER-derived PBs.

Key words: Endoplasmic reticulum, Oryza sativa, prolamin, protein body, storage protein, transgenic rice

Received 22 July 2008; Revised 22 October 2008 Accepted 10 November 2008


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